Fig. 2: Design of allosterically controlled cyclic assemblies.

a, Design models in the unbound Xm oligomeric state (pink). b, Design models in the peptide (P)-bound Yn oligomeric state (blue, protein; red, effector peptide). c, nsEM 2D class averages for designs in the absence (left) and presence (right) of peptide representing top views of the predominant oligomeric species by particle count. d, SEC on each design at 5 μM in the absence (pink) and presence (blue) of 10 μM untagged peptide. e, MP on these designs at 100 nM final protein concentration in the absence (left) and presence (right) of tenfold molar excess of peptide. f, Characterization of sr508, with data following column organization of a–e, from left to right: design model in the unbound X2 state, design model in the bound Y2P4 state, nsEM 2D class averages for sr508 in the absence (left) and presence (right) of peptide, SEC on sr508 in the absence of peptide (blue), the presence of untagged peptide (pink) and GFP-tagged peptide (green), MP on sr508 in the absence (left) and presence (right) of untagged peptide. Norm., normalized. Scale bars: 250 Å (c), 200 Å (f).